ID   PP2A4_YEAST             Reviewed;         368 AA.
AC   P32838; D6W1K6; E9P8U5;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   27-MAR-2024, entry version 191.
DE   RecName: Full=Serine/threonine-protein phosphatase PP2A-like PPG1;
DE            EC=3.1.3.16;
GN   Name=PPG1; Synonyms=PPG; OrderedLocusNames=YNR032W; ORFNames=N3281;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7678255; DOI=10.1016/s0021-9258(18)54082-5;
RA   Posas F., Clotet J., Muns M.T., Corominas J., Casamayor A., Arino J.;
RT   "The gene PPG encodes a novel yeast protein phosphatase involved in
RT   glycogen accumulation.";
RL   J. Biol. Chem. 268:1349-1354(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   INTERACTION WITH TAP42.
RX   PubMed=14551259; DOI=10.1091/mbc.e03-02-0072;
RA   Wang H., Wang X., Jiang Y.;
RT   "Interaction with Tap42 is required for the essential function of Sit4 and
RT   type 2A phosphatases.";
RL   Mol. Biol. Cell 14:4342-4351(2003).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   INTERACTION WITH PPE1 AND RRD1.
RX   PubMed=15447631; DOI=10.1042/bj20040887;
RA   Van Hoof C., Martens E., Longin S., Jordens J., Stevens I., Janssens V.,
RA   Goris J.;
RT   "Specific interactions of PP2A and PP2A-like phosphatases with the yeast
RT   PTPA homologues, Ypa1 and Ypa2.";
RL   Biochem. J. 386:93-102(2005).
CC   -!- FUNCTION: Involved in glycogen accumulation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Inactivated in a complex with phosphatase methylesterase PPE1
CC       (PP2Ai). Interacts with phosphatase 2A activator RRD1, which can
CC       reactivate PP2Ai by dissociating the catalytic subunit from the
CC       complex. Interacts with TAP42. {ECO:0000269|PubMed:14551259,
CC       ECO:0000269|PubMed:15447631}.
CC   -!- PTM: Reversibly methyl esterified on Leu-368 by leucine carboxyl
CC       methyltransferase 1 (PPM1) and protein phosphatase methylesterase 1
CC       (PPE1). Carboxyl methylation influences the affinity of the catalytic
CC       subunit for the different regulatory subunits, thereby modulating the
CC       PP2A holoenzyme's substrate specificity, enzyme activity and cellular
CC       localization.
CC   -!- MISCELLANEOUS: Present with 1960 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2A subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M94269; AAA34895.1; -; Genomic_DNA.
DR   EMBL; Z71647; CAA96312.1; -; Genomic_DNA.
DR   EMBL; AY558021; AAS56347.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10572.1; -; Genomic_DNA.
DR   PIR; S63363; S63363.
DR   RefSeq; NP_014429.3; NM_001183209.3.
DR   AlphaFoldDB; P32838; -.
DR   SMR; P32838; -.
DR   BioGRID; 35856; 228.
DR   DIP; DIP-1523N; -.
DR   IntAct; P32838; 9.
DR   MINT; P32838; -.
DR   STRING; 4932.YNR032W; -.
DR   MaxQB; P32838; -.
DR   PaxDb; 4932-YNR032W; -.
DR   PeptideAtlas; P32838; -.
DR   TopDownProteomics; P32838; -.
DR   EnsemblFungi; YNR032W_mRNA; YNR032W; YNR032W.
DR   GeneID; 855766; -.
DR   KEGG; sce:YNR032W; -.
DR   AGR; SGD:S000005315; -.
DR   SGD; S000005315; PPG1.
DR   VEuPathDB; FungiDB:YNR032W; -.
DR   eggNOG; KOG0372; Eukaryota.
DR   GeneTree; ENSGT00960000189235; -.
DR   HOGENOM; CLU_004962_8_1_1; -.
DR   InParanoid; P32838; -.
DR   OMA; HQLCMDG; -.
DR   OrthoDB; 19833at2759; -.
DR   BioCyc; YEAST:G3O-33343-MONOMER; -.
DR   BioGRID-ORCS; 855766; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P32838; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P32838; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0090443; C:FAR/SIN/STRIPAK complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0061509; P:asymmetric protein localization to old mitotic spindle pole body; IBA:GO_Central.
DR   GO; GO:0005977; P:glycogen metabolic process; IMP:SGD.
DR   CDD; cd07415; MPP_PP2A_PP4_PP6; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR047129; PPA2-like.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR45619; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A-RELATED; 1.
DR   PANTHER; PTHR45619:SF6; SERINE_THREONINE-PROTEIN PHOSPHATASE PP2A-LIKE PPG1; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF033096; PPPtase_5; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Manganese; Metal-binding; Methylation; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..368
FT                   /note="Serine/threonine-protein phosphatase PP2A-like PPG1"
FT                   /id="PRO_0000058876"
FT   ACT_SITE        111
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         50
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         52
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        126
FT                   /note="C -> S (in Ref. 1; AAA34895)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        154
FT                   /note="D -> G (in Ref. 4; AAS56347)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   368 AA;  42433 MW;  1B326BBC41A67481 CRC64;
     MELDECLERL YKAQLLPEVT VRALCFKLKE MLVKESNVIH IQTPVTVVGD MHGQFHDMLE
     IFQIGGPVPD TNYLFLGDYV DRGLYSVETI MLLIVLKLRY PSRIHLLRGN HESRQITQSY
     GFYTECLNKY GGNSRVWQYL TDIFDYLVLC CIIDDEIFCV HGGLSPNVQT IDQIKIIDRF
     REIPHDGAMA DLVWSDPEEN NNPTLDHPDN SGQHFQVSPR GAGYTFGRSV VEKFLRMNDM
     NRIYRAHQLC NEGYQIYFDG LVTTVWSAPN YCYRCGNKAS ILELYSKDQF YFNVFEEAPE
     NKLLKENSMN DNALEDSISN PVANRKLIAD YFEDDSASAD GSTDPEMYIF SDVYQARSAS
     NRHVDYFL
//